ID A0A1P8YFZ4_9NOCA Unreviewed; 556 AA.
AC A0A1P8YFZ4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=acetolactate synthase {ECO:0000256|ARBA:ARBA00013145};
DE EC=2.2.1.6 {ECO:0000256|ARBA:ARBA00013145};
GN ORFNames=BTZ20_4109 {ECO:0000313|EMBL:AQA23034.1};
OS Rhodococcus sp. MTM3W5.2.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1805827 {ECO:0000313|EMBL:AQA23034.1, ECO:0000313|Proteomes:UP000187995};
RN [1] {ECO:0000313|EMBL:AQA23034.1, ECO:0000313|Proteomes:UP000187995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MTM3W5.2 {ECO:0000313|EMBL:AQA23034.1,
RC ECO:0000313|Proteomes:UP000187995};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2;
CC Xref=Rhea:RHEA:25249, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:58476; EC=2.2.1.6;
CC Evidence={ECO:0000256|ARBA:ARBA00000673};
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC isoleucine from 2-oxobutanoate: step 1/4.
CC {ECO:0000256|ARBA:ARBA00004974}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC pyruvate: step 1/4. {ECO:0000256|ARBA:ARBA00005025}.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP019572; AQA23034.1; -; Genomic_DNA.
DR RefSeq; WP_077042317.1; NZ_CP019572.1.
DR AlphaFoldDB; A0A1P8YFZ4; -.
DR STRING; 1805827.BTZ20_4109; -.
DR OrthoDB; 2254214at2; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000187995; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00568; TPP_enzymes; 1.
DR CDD; cd07035; TPP_PYR_POX_like; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF13; ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL; 1.
DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 14..125
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 205..301
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 391..539
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 556 AA; 58052 MW; F3D4D8E904CA1093 CRC64;
MGMSGRAHGN TQRRVVDYLV DSVTALGVRH IFGVDGANIE DLYDAIFDAG VDVTGVVAKH
EFSAVTMADG YARSTSGLGV VAATSGGGAM NLVAGLAESF TSRVPVLAVV GQPPTASEGN
GAFQDSSGRA GSINAVRLFS EISRYCARVE RPEDIAEHLQ RAVSAARRGG PGVLLLPKDV
QQATVTVPRF TPPARRVVHD RIGLARVTAM IAEARRTGKI VLVVGDQVAR NDARPQLRAL
AVALDAAVGV APDAKDCYTP DERGFCGVAG TMGHAELVDA VRQSALCLLV GTRMPMTARA
GLDGALAAVP VASIGAEPPY LPTTHAVGMN LGSTLADLAA VFHSDGEPEP AAPQALTTLE
VPDSSGPGLR YREAVEAIGA MLPSGSDVFA DAGNTGASVV HHLSAPRGGR FVVALGMGGM
GYSFGAGIGS AFTRNRRTFV IAGDGAFFMH GLEIHTAIEH NLPVTFIIFN NNAHAMCVTR
EQLFYRNRYS FNRFRPTLLG EGIAAMFPTL SAFAARSAGD LTDALARSAH TEGPSFVSVD
CDPDEIPPFL PFLTHP
//
